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- EMDB-49267: SNF2H bound to nucleosome - Class E1 -

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Basic information

Entry
Database: EMDB / ID: EMD-49267
TitleSNF2H bound to nucleosome - Class E1
Map dataSNF2H bound to nucleosome - Class E1
Sample
  • Complex: SNF2H bound to nucleosome - Class E1
    • Other: Histone H3
    • Other: Histone H4
    • Other: Histone H2A
    • Other: Histone H2B
    • Other: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5/SNF2H
    • DNA: Chain I
    • DNA: Chain J
KeywordsChromatin / remodeler / DNA BINDING PROTEIN
Function / homology
Function and homology information


RSF complex / histone octamer slider activity / ACF complex / WICH complex / negative regulation of mitotic chromosome condensation / CERF complex / CHRAC / NoRC complex / NURF complex / nucleosome array spacer activity ...RSF complex / histone octamer slider activity / ACF complex / WICH complex / negative regulation of mitotic chromosome condensation / CERF complex / CHRAC / NoRC complex / NURF complex / nucleosome array spacer activity / B-WICH complex / rDNA heterochromatin formation / ATP-dependent chromatin remodeler activity / chromatin silencing complex / negative regulation of transcription by RNA polymerase I / positive regulation of transcription by RNA polymerase III / DNA methylation-dependent constitutive heterochromatin formation / positive regulation of transcription by RNA polymerase I / regulation of DNA replication / pericentric heterochromatin / nucleosome binding / condensed chromosome / antiviral innate immune response / Deposition of new CENPA-containing nucleosomes at the centromere / cellular response to leukemia inhibitory factor / positive regulation of DNA replication / meiotic cell cycle / DNA-templated transcription initiation / helicase activity / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / fibrillar center / structural constituent of chromatin / nucleosome / heterochromatin formation / nucleosome assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / site of double-strand break / chromosome / chromatin organization / DNA recombination / chromatin remodeling / protein heterodimerization activity / DNA repair / DNA damage response / centrosome / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / chromatin / nucleolus / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / nucleus
Similarity search - Function
ISWI, HAND domain / SLIDE domain / ISWI, HAND domain superfamily / HAND / SLIDE / SANT domain profile. / SANT domain / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal ...ISWI, HAND domain / SLIDE domain / ISWI, HAND domain superfamily / HAND / SLIDE / SANT domain profile. / SANT domain / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / : / Histone H2B signature. / Histone H2A conserved site / Histone H2A signature. / Histone H2B / Histone H2B / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone 2A / Histone H2A / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Homeobox-like domain superfamily / Helicase conserved C-terminal domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 domain / Histone-fold / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 / Histone H2B 1.1 / Histone H4 / Histone H3.2 / Histone H2AX
Similarity search - Component
Biological speciesHomo sapiens (human) / Xenopus laevis (African clawed frog) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsMalik D / Deshmukh AA / Bilokapic S / Halic M
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R01GM135599-01 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM141694-01 United States
CitationJournal: Cell Res / Year: 2025
Title: Mechanisms of chromatin remodeling by the human Snf2-type ATPase SNF2H.
Authors: Deepshikha Malik / Ashish Deshmukh / Silvija Bilokapic / Mario Halic /
History
DepositionFeb 17, 2025-
Header (metadata) releaseJun 4, 2025-
Map releaseJun 4, 2025-
UpdateJun 18, 2025-
Current statusJun 18, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_49267.png

Downloads & links

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Map

FileDownload / File: emd_49267.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSNF2H bound to nucleosome - Class E1
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.3 Å/pix.
x 384 pix.
= 498.048 Å		1.3 Å/pix.
x 384 pix.
= 498.048 Å		1.3 Å/pix.
x 384 pix.
= 498.048 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.297 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0083
Minimum - Maximum-0.02764291 - 0.050022542
Average (Standard dev.)-0.000027195389 (±0.0022834244)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 498.04803 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half Map A

Fileemd_49267_half_map_1.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map B

Fileemd_49267_half_map_2.map
AnnotationHalf Map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : SNF2H bound to nucleosome - Class E1

EntireName: SNF2H bound to nucleosome - Class E1
Components
  • Complex: SNF2H bound to nucleosome - Class E1
    • Other: Histone H3
    • Other: Histone H4
    • Other: Histone H2A
    • Other: Histone H2B
    • Other: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5/SNF2H
    • DNA: Chain I
    • DNA: Chain J

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Supramolecule #1: SNF2H bound to nucleosome - Class E1

SupramoleculeName: SNF2H bound to nucleosome - Class E1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Histone H3

MacromoleculeName: Histone H3 / type: other / ID: 1 / Classification: other
Source (natural)Organism: Xenopus laevis (African clawed frog)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA

UniProtKB: Histone H3.2
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #2: Histone H4

MacromoleculeName: Histone H4 / type: other / ID: 2 / Classification: other
Source (natural)Organism: Xenopus laevis (African clawed frog)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG

UniProtKB: Histone H4
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #3: Histone H2A

MacromoleculeName: Histone H2A / type: other / ID: 3 / Classification: other
Source (natural)Organism: Xenopus laevis (African clawed frog)
SequenceString:
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGR VTIAQGGVLP NIQSVLLPKK TESSKSAKSK

UniProtKB: Histone H2AX
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #4: Histone H2B

MacromoleculeName: Histone H2B / type: other / ID: 4 / Classification: other
Source (natural)Organism: Xenopus laevis (African clawed frog)
SequenceString:
MPEPAKSAPA PKKGSKKAVT KTQKKDGKKR RKSRKESYAI YVYKVLKQVH PDTGISSKAM SIMNSFVNDV FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSAK

UniProtKB: Histone H2B 1.1
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #5: SWI/SNF-related matrix-associated actin-dependent regulator of ch...

MacromoleculeName: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5/SNF2H
type: other / ID: 5 / Classification: other
Source (natural)Organism: Homo sapiens (human)
SequenceString: MSSAAEPPPP PPPESAPSKP AASIASGGSN SSNKGGPEGV AAQAVASAAS AGPADAEMEE IFDDASPGKQ KEIQEPDPTY EEKMQTDRAN RFEYLLKQTE LFAHFIQPAA QKTPTSPLKM KPGRPRIKKD EKQNLLSVGD YRHRRTEQEE DEELLTESSK ATNVCTRFED ...String:
MSSAAEPPPP PPPESAPSKP AASIASGGSN SSNKGGPEGV AAQAVASAAS AGPADAEMEE IFDDASPGKQ KEIQEPDPTY EEKMQTDRAN RFEYLLKQTE LFAHFIQPAA QKTPTSPLKM KPGRPRIKKD EKQNLLSVGD YRHRRTEQEE DEELLTESSK ATNVCTRFED SPSYVKWGKL RDYQVRGLNW LISLYENGIN GILADEMGLG KTLQTISLLG YMKHYRNIPG PHMVLVPKST LHNWMSEFKR WVPTLRSVCL IGDKEQRAAF VRDVLLPGEW DVCVTSYEML IKEKSVFKKF NWRYLVIDEA HRIKNEKSKL SEIVREFKTT NRLLLTGTPL QNNLHELWSL LNFLLPDVFN SADDFDSWFD TNNCLGDQKL VERLHMVLRP FLLRRIKADV EKSLPPKKEV KIYVGLSKMQ REWYTRILMK DIDILNSAGK MDKMRLLNIL MQLRKCCNHP YLFDGAEPGP PYTTDMHLVT NSGKMVVLDK LLPKLKEQGS RVLIFSQMTR VLDILEDYCM WRNYEYCRLD GQTPHDERQD SINAYNEPNS TKFVFMLSTR AGGLGINLAT ADVVILYDSD WNPQVDLQAM DRAHRIGQTK TVRVFRFITD NTVEERIVER AEMKLRLDSI VIQQGRLVDQ NLNKIGKDEM LQMIRHGATH VFASKESEIT DEDIDGILER GAKKTAEMNE KLSKMGESSL RNFTMDTESS VYNFEGEDYR EKQKIAFTEW IEPPKRERKA NYAVDAYFRE ALRVSEPKAP KAPRPPKQPN VQDFQFFPPR LFELLEKEIL FYRKTIGYKV PRNPELPNAA QAQKEEQLKI DEAESLNDEE LEEKEKLLTQ GFTNWNKRDF NQFIKANEKW GRDDIENIAR EVEGKTPEEV IEYSAVFWER CNELQDIEKI MAQIERGEAR IQRRISIKKA LDTKIGRYKA PFHQLRISYG TNKGKNYTEE EDRFLICMLH KLGFDKENVY DELRQCIRNS PQFRFDWFLK SRTAMELQRR CNTLITLIER ENMELEEKEK AEKKKRGPKP STQKRKMDGA PDGRGRKKKL KL

UniProtKB: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #6: Chain I

MacromoleculeName: Chain I / type: dna / ID: 6 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
SequenceString:
ACAGGATGTA TATATCTGAC ACGTGCCTGG AGACTAGGGA GTAATCCCCT TGGCGGtTAA AACGCGGGGG ACAGCGCGTA CGTGCGTTTA AGCGGTGCTA GAGCTGTCTA CGACCAATTG AGCGGCCTCG GCACCGGGAT TCTCCAGGG

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Macromolecule #7: Chain J

MacromoleculeName: Chain J / type: dna / ID: 7 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
SequenceString:
CCCTGGAGAA TCCCGGTGCC GAGGCCGCTC AATTGGTCGT AGACAGCTCT AGCACCGCTT AAACGCACGT ACGCGCTGTC CCCCGCGTTT TAaCCGCCAA GGGGATTACT CCCTAGTCTC CAGGCACGTG TCAGATATAT ACATCCTGTG CA

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 30 sec.
VitrificationCryogen name: ETHANE / Chamber temperature: 285.65 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
TemperatureMin: 160.0 K / Max: 175.0 K
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 61.6 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: EMDB MAP
EMDB ID:

21970

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 7000
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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